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Conserved domains on  [gi|193211330|ref|NP_001122751|]
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Palmitoyltransferase [Caenorhabditis elegans]

Protein Classification

DHHC family palmitoyltransferase( domain architecture ID 10479004)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes

EC:  2.3.1.-
Gene Ontology:  GO:0016409|GO:0043543|GO:0016747
PubMed:  21388813|32522557|21204476

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 129-272 3.11e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


:

Pssm-ID: 396215  Cd Length: 132  Bit Score: 120.55  E-value: 3.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330  129 HGIRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILFLAYGFIFCIWIAATTLPSFIDFWRHEYD 208
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193211330  209 mnkkqydsIDSVIQRNLKHLHTVLSNGRFPLVFLLFLSCmfslslsflffYHLYLTAKNRTTVE 272
Cdd:pfam01529  83 --------FFFLILFLFSISIILLILSLFFLLFLGILLF-----------FHLYLISRNLTTYE 127
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 129-272 3.11e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 120.55  E-value: 3.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330  129 HGIRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILFLAYGFIFCIWIAATTLPSFIDFWRHEYD 208
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193211330  209 mnkkqydsIDSVIQRNLKHLHTVLSNGRFPLVFLLFLSCmfslslsflffYHLYLTAKNRTTVE 272
Cdd:pfam01529  83 --------FFFLILFLFSISIILLILSLFFLLFLGILLF-----------FHLYLISRNLTTYE 127
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
22-321 2.13e-25

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 104.45  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330  22 FLPVVLVSLATGWGIYAYtyelcILSIDNWPQRIIYLFIFYALLILFYTSYLRTVYTKAWKPPQKYCIEGASKATYESVK 101
Cdd:COG5273   31 FIGLFLLSRIVVYTLLVI-----VKSLSLVVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLSGYRETISRLLDDGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 102 DDERqlqlflsdiarerdltllvrgfdhgiRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILFL 181
Cdd:COG5273  106 FGTE--------------------------NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 182 AYgFIFCIWIAATTLPSFIDFWRHEYdmnkKQYDSIDSVIqrnlkhlhtVLSNGRFPLVFLLFLSCmfslslsfLFFYHL 261
Cdd:COG5273  160 LY-TILVALVVLLSTAYYIAGIFSIR----HDTSLAICFL---------IFGCSLLGVVFFIITTL--------LLLFLI 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 262 YLTAKNRTTVESFRapMIDGKYAKDAFNH-----------------------GIRANYREIFGSHPLYWFLPVPSSLGDG 318
Cdd:COG5273  218 YLILNNLTTIEFIQ--ISRGGSTLEFFPLcresnlpftnifdssegalpldlGIGQNLSTIKGSNALYWLTPLHTNYCNS 295


                 ...
gi 193211330 319 VEF 321
Cdd:COG5273  296 YDF 298
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 129-272 3.11e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 120.55  E-value: 3.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330  129 HGIRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILFLAYGFIFCIWIAATTLPSFIDFWRHEYD 208
Cdd:pfam01529   3 DELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193211330  209 mnkkqydsIDSVIQRNLKHLHTVLSNGRFPLVFLLFLSCmfslslsflffYHLYLTAKNRTTVE 272
Cdd:pfam01529  83 --------FFFLILFLFSISIILLILSLFFLLFLGILLF-----------FHLYLISRNLTTYE 127
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
22-321 2.13e-25

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 104.45  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330  22 FLPVVLVSLATGWGIYAYtyelcILSIDNWPQRIIYLFIFYALLILFYTSYLRTVYTKAWKPPQKYCIEGASKATYESVK 101
Cdd:COG5273   31 FIGLFLLSRIVVYTLLVI-----VKSLSLVVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLSGYRETISRLLDDGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 102 DDERqlqlflsdiarerdltllvrgfdhgiRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILFL 181
Cdd:COG5273  106 FGTE--------------------------NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 182 AYgFIFCIWIAATTLPSFIDFWRHEYdmnkKQYDSIDSVIqrnlkhlhtVLSNGRFPLVFLLFLSCmfslslsfLFFYHL 261
Cdd:COG5273  160 LY-TILVALVVLLSTAYYIAGIFSIR----HDTSLAICFL---------IFGCSLLGVVFFIITTL--------LLLFLI 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211330 262 YLTAKNRTTVESFRapMIDGKYAKDAFNH-----------------------GIRANYREIFGSHPLYWFLPVPSSLGDG 318
Cdd:COG5273  218 YLILNNLTTIEFIQ--ISRGGSTLEFFPLcresnlpftnifdssegalpldlGIGQNLSTIKGSNALYWLTPLHTNYCNS 295


                 ...
gi 193211330 319 VEF 321
Cdd:COG5273  296 YDF 298
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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